title: Isolation and some properties of bovine brain 100 kDa heat shock protein.
abstract: 1. The 100 kDa protein was purified from bovine brains. 2. The antibody against the 100 kDa brain protein was prepared and was monospecific to the antigen. 3. The antibody cross-reacted with HeLa cell HSP100 (100 kDa heat shock protein). 4. The physicochemical, immunochemical properties and a partially amino acid sequence indicated that the 100 kDa protein was HSP100. 5. Peptide mapping using Staphylococcus aureus V8 protease showed a core peptide with 10 kDa molecular mass common to both HSP100 and HSP90. 6. The amino acid sequence of the 10 kDa fragment of the 100 kDa protein showed a high homology with that of human HSP90 (38-60); the difference was only two of 23 amino acid residues determined.
authors.affiliation: Department of Biochemistry, Akita University School of Medicine, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Itoh
authors.forename: R
authors.initials: R
authors.lastname: Kobayashi
authors.forename: Y
authors.initials: Y
authors.lastname: Tashima
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D001923:Brain Chemistry; D002417:Cattle; D002850:Chromatography, Gel; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D012689:Sequence Homology, Nucleic Acid
chemical_list: D006360:Heat-Shock Proteins